sialyl lewis x

Sialyl Lewis X-Lactose, a biochemical reagent, serves as a biological material or organic compound for life science research.

Sialyl-Lewis X (sLeX), a sialylated fucosylated tetrasaccharide and endogenous antigen, serves as a high-affinity ligand for selectins (E-, P-, and L-selectin)[1]. It interacts with ELAM-1 and CD62, consequently inhibiting CD62-mediated neutrophil recruitment to inflammation sites[2].

Fucosyltransferase 6 is an enzyme responsible for the expression of the tetrasaccharide Sialyl-Lewis x (sLex, CD15s) on the surface of leukocytes. The sLex structure is crucial for E-selectin-mediated leukocyte rolling, which is associated with leukocyte extravasation from blood vessels.

Focusyltransferase 7 (FUT7) is a Golgi stack membrane protein. It catalyzes the final fucosylation step in the synthesis of Lewis antigens, resulting in the production of the specific glycosylated product sialyl Lewis X (sLeX). FUT7 is involved in catalyzing the α-1,3 glycosidic bond, which is crucial for sialyl Lewis X antigen expression.